Dipeptidyl peptidase IV production by solid state fermentation using alternative fungal sources
The present work was carried out for the production of dipeptidyl peptidase IV (DPP IV; EC 3.4.14.5) using Aspergillus, Penicillium, and Rhizopus strains under solid state fermentation conditions. Response surface methodology was applied for the optimization of the selected operational variables (corn flour, initial moisture content, and cultivation time) for DPP IV activity as the response. The optimal parameters of DPP IV activity for the independent variables, namely the amount of corn flour (% w/w), initial moisture content (% w/w), and cultivation time (days), were evaluated to be 2.44%, 60.85%, and 4.69 days, respectively, using Aspergillus awamori T116. The response for these results was also shown to be in very close agreement with the experimental data.
Dipeptidyl peptidase IV production by solid state fermentation using alternative fungal sources
The present work was carried out for the production of dipeptidyl peptidase IV (DPP IV; EC 3.4.14.5) using Aspergillus, Penicillium, and Rhizopus strains under solid state fermentation conditions. Response surface methodology was applied for the optimization of the selected operational variables (corn flour, initial moisture content, and cultivation time) for DPP IV activity as the response. The optimal parameters of DPP IV activity for the independent variables, namely the amount of corn flour (% w/w), initial moisture content (% w/w), and cultivation time (days), were evaluated to be 2.44%, 60.85%, and 4.69 days, respectively, using Aspergillus awamori T116. The response for these results was also shown to be in very close agreement with the experimental data.
___
- Aleksandra EN, Ivana Z, Matić MD et al. Serum DPP IV activity and CD26 expression on lymphocytes in patients with benign or malignant breast tumors. Immunobiology 216: 942- 946, 2011.
- Wasilewska J, Sienkiewicz-Szłapka E, Kuźbida E et al. The exogenous opioid peptides and DPP IV serum activity in infants with apnoea expressed as apparent life threatening events (ALTE). Neuropeptides 45: 189-195, 2011.
- Andrade CF, Bigni R, Pombo-de-Oliveira MS et al. CD26/DPP IV cell membrane expression and DPP IV activity in plasma of patients with acute leukemia. J Enzyme Inhib Med Chem 24: 708-714, 2009.
- Bergmann A, Bohuon C. Decrease of serum dipeptidyl peptidase activity in severe sepsis patients: relationship to procalcitonin. Clin Chim Acta 321: 23-126, 2002.
- Lambeir AM, Proost P, Scharpé SD et al. A kinetic study of glucagon-like peptide-1 and glucagon-like peptide-2 truncation by dipeptidyl peptidase IV, in vitro. Biochem Pharmacol 64: 1753-1756, 2002.
- Keane NM, Price P, Lee S et al. An evaluation of serum soluble CD30 levels and serum CD26 (DPP IV) enzyme activity as markers of type 2 and type 1 cytokines in HIV patients receiving highly active antiretroviral therapy. Clin Exp Immunol 126: 111-116, 2001.
- Iwaki-Egawa S, Watanabe Y, Kikuya Y et al. DPP IV from human serum: purification, characterization, and N-terminal amino acid sequence. J Biochem 124: 428-433, 1998.
- Urade M, Uematsu T, Mima T et al. Serum dipeptidyl peptidase (DPP) IV activity in hamster buccal pouch carcinogenesis with 9,10-dimethyl-1,2-benzanthracene. J Oral Pathol Med 21: 109- 112, 1992.
- Püschel G, Mentlein R, Heymann E. Isolation and characterisation of dipeptidyl peptidase IV from human placenta. Eur J Biochem 126: 359-365, 1982.
- Cunningham DF, O’Connor B. Proline specific peptidases. Biochim Bophys Acta 1343: 160-186, 1997.
- Mentlein R. Dipeptidyl peptidase IV (CD26) - role in the inactivation of regulatory peptides. Regul Pept 85: 2-4, 1999.
- Baum O, Reuter W, Bermpohl F. Structure function relationship of DPP IV: insight into its dimerisation and gelatinase activity. Adv Exp Med Biol 524: 19-27, 2004.
- Iwan M, Jarmolowska B, Bielkowicz K et al. Transport of µ-opioid receptor agonists and antagonist peptides across Caco-2 monolayer. Peptides 29: 1042-1047, 2008.
- Hunter LC, O’Hare A, Herron WJ et al. Opioid peptides and dipeptidyl peptidase in autism. Dev Med Child Neurol 45: 121- 128, 2003.
- Cade R, Privette R, Fregly M et al. Autism and schizophrenia: intestinal disorders. Nutr Neurosci 3: 53-72, 2000.
- Reichelt KL, Knivsberg AM, Nodland M. Nature and consequences of hyperpetiduria and bovine casomorphins found in autistic syndromes. Dev Brain Dysfunc 7: 71-85, 1994.
- Marchetti B, Scifo R, Batticane N et al. Immunological significance of opioid peptide dysfunction in infantile autism. Brain Dysfunc 3: 346-354, 1990.
- Reichelt K, Hole K, Hamberger A et al. Biologically active peptide-containing fractions in schizophrenia and childhood autism. Adv Biochem Psycopharmacol 28: 627-643, 1981.
- Thoma R, Löffler B, Stihle M et al. Structural basis of proline- specific exopeptidase activity as observed in human dipeptidyl peptidase IV. Structure 11: 947-959, 2003.
- Brudnak MA. Composition and method for increasing exorphin catabolism to treat autism. United States Patent, Patent No. 6,783,757, 2004.
- Brudnak MA, Rimland B, Kerry RE et al. Enzyme-based therapy for autism spectrum disorders - is it worth another look? Med Hypotheses 58: 422-428, 2002.
- Houston DB. Compositions and methods relating to reduction of symptoms of autism. United States Patent, Patent No. 6,808,708, 2004.
- Wakefield AJ, Walker-Smith JA, Murch SH. Colonic CD8 and gamma t-cell infiltration with epithelial damage in children with autism. J Pediatr 138: 366-372, 2001.
- Horvalt K, Papadimitriou JC, Rabsztyn A et al. Gastrointestinal abnormalities in children with autistic disorder. J Pediatr 135: 533-535, 1999.
- Johnson CR, Handen BL, Zimmer M et al.Effects of gluten free / casein free diet in young children with autism: a pilot study. J Dev Phys Disabil 23: 213-225, 2011.
- Christison GW, Ivany K. Elimination diets in autism spectrum disorders: any wheat amidst the chaff? J Dev Behav Pediatr 27: 162-171, 2006.
- Knivsberg AM, Reichelt, KL Nodland M. Reports on dietary intervention in autistic disorders. Nutr Neourosci 4: 25-37, 2001.
- Perez-Guzman AE, Victoria TC, Cruz-Camarillo R et al. Improvement of fermentation conditions for the production of X-prolyl-dipeptidyl aminopeptidase from Lactococcus lactis. Word J Microbiol Biotechnol 20: 413-417, 2004.
- Zevaco C, Monnet V, Gripon JC. Intracellular X-prolyl dipeptidyl peptidase from Lactococcus lactis spp. lactis: purification and properties. J Appl Bacteriol 68: 357-366, 1990.
- Tachi H, Ito H, Ichishima E. An X-prolyl dipeptidyl- aminopeptidase from Aspergillus oryzae. Phytochemistry 31: 3707-3709, 1992.
- Doumas A, Van den Broek B, Affolter M et al. Characterization of the prolyl dipeptidyl peptidase gene (DPP IV) from the Koji mold Aspergillus oryzae. Appl Environ Microbiol 64: 4809- 4815, 1998.
- Jalving R, Godefrooij J, Veen WJ et al. Characterisation of the Aspergillus niger dapB gene, which encodes a novel fungal type IV dipeptidyl aminopeptidase. Mol Genet Genomics 27: 319- 325, 2005.
- Beauvais A, Monod, M, Debeaupuis JD et al. Biochemical and antigenic characterization of a new dipeptidyl-peptidase isolated from Aspergillus fumigatus. J Biol Chem 272: 6238- 6244, 1997.
- Sigma-Aldrich. Enzymatic Assay of Dipeptidyl Peptidase IV (EC 3.4.14.5), SSGPNA01, 2006 Revised: 08/26/99:1-2. Sigma- Aldrich. St. Louis; 2006.
- Monod ML, Doumas G, Pully AM et al. Cloning of the prolyl- dipeptidyl-peptidase from Aspergillus oryzae. United States Patent, Patent No. 6,309,868 B1, 2001.